Dynamin-like MxA GTPase: Structural insights into oligomerization and implications for antiviral activity


  • O. Haller
  • S. Gao
  • A. von der Malsburg
  • O. Daumke
  • G. Kochs


  • Journal of Biological Chemistry


  • J Biol Chem 285 (37): 28419-28424


  • The interferon-inducible MxA GTPase is a key mediator of cell-autonomous innate immunity against a broad range of viruses, such as influenza and bunyaviruses. MxA shares a similar domain structure with the dynamin superfamily of mechano-chemical enzymes, including an amino-terminal GTPase domain (G domain), a central middle domain (MD) and a carboxy-terminal GTPase effector domain (GED). Recently, crystal structures of a G domain dimer of dynamin 1 and of the oligomerised stalk of MxA (built by the MD and GED) were determined. These data provide exciting insights into the architecture and antiviral function of the MxA oligomer. Moreover, the structural knowledge paves the way for the development of novel antivirals against influenza and other highly pathogenic viruses.